ID   RUTD_ECOKI              Reviewed;         266 AA.
AC   D5CZG9;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Putative carbamate hydrolase RutD {ECO:0000255|HAMAP-Rule:MF_00832};
DE            EC=3.5.1.- {ECO:0000255|HAMAP-Rule:MF_00832};
DE   AltName: Full=Aminohydrolase {ECO:0000255|HAMAP-Rule:MF_00832};
GN   Name=rutD {ECO:0000255|HAMAP-Rule:MF_00832}; OrderedLocusNames=ECOK1_1061;
OS   Escherichia coli O18:K1:H7 (strain IHE3034 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=714962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHE3034 / ExPEC;
RX   PubMed=20439758; DOI=10.1073/pnas.0915077107;
RA   Moriel D.G., Bertoldi I., Spagnuolo A., Marchi S., Rosini R., Nesta B.,
RA   Pastorello I., Corea V.A., Torricelli G., Cartocci E., Savino S.,
RA   Scarselli M., Dobrindt U., Hacker J., Tettelin H., Tallon L.J.,
RA   Sullivan S., Wieler L.H., Ewers C., Pickard D., Dougan G., Fontana M.R.,
RA   Rappuoli R., Pizza M., Serino L.;
RT   "Identification of protective and broadly conserved vaccine antigens from
RT   the genome of extraintestinal pathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:9072-9077(2010).
CC   -!- FUNCTION: Involved in pyrimidine catabolism. May facilitate the
CC       hydrolysis of carbamate, a reaction that can also occur spontaneously.
CC       {ECO:0000255|HAMAP-Rule:MF_00832}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamate + 2 H(+) = CO2 + NH4(+); Xref=Rhea:RHEA:15649,
CC         ChEBI:CHEBI:13941, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:28938; Evidence={ECO:0000255|HAMAP-Rule:MF_00832};
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Hydrolase RutD
CC       family. {ECO:0000255|HAMAP-Rule:MF_00832}.
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DR   EMBL; CP001969; ADE91095.1; -; Genomic_DNA.
DR   RefSeq; WP_001331944.1; NC_017628.1.
DR   AlphaFoldDB; D5CZG9; -.
DR   SMR; D5CZG9; -.
DR   ESTHER; ecoli-rutD; RutD.
DR   KEGG; eih:ECOK1_1061; -.
DR   PATRIC; fig|714962.3.peg.1075; -.
DR   HOGENOM; CLU_020336_50_1_6; -.
DR   OMA; HAMSVTD; -.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0019740; P:nitrogen utilization; IEA:UniProtKB-UniRule.
DR   GO; GO:0006212; P:uracil catabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_00832; RutD; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR019913; Pyrimidine_utilisation_RutD.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR03611; RutD; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..266
FT                   /note="Putative carbamate hydrolase RutD"
FT                   /id="PRO_0000402955"
SQ   SEQUENCE   266 AA;  28878 MW;  506FAC2B78E541CA CRC64;
     MKLSLSPPPY ADAPVVVLIS GLGGSGSYWL PQLAVLVQEY QVVCYDQRGT GNNPDTLAED
     YSIAQMAAEL HQALVAAGIE RYAVVGHALG ALVGMQLALD YPASVTVLVS VNGWLRINAH
     TRRCFQVREQ LLHSGGAQAW VEAQPLFLYP ADWMAARAPR LEAEDALALA HFQGKNNLLR
     RLNALKRADF SHHADRIRCP VQIICASDDL LVPTACSSEL HAALPDSQKM VMRYGGHACN
     VTDPETFNAL LLNGLASLLH HREAAL